Discursive Objects

17-25 October 2015, 11h – 18h Gagelstraat 44, 5616RR, EIndhoven Aldo Bakker, Maarten Baas, David Bernstein, Martin John Callanan, Chmara Rosinke, Sarah Daher & guests, The Grantchester Pottery, Richard Healy, Anton Hjertstedt, Vincent Knopper, Pieteke Korte, Nynke Koster, Pottery Yacht Club, Corinne Mynatt, n-o-m-a-n, Studio Minale Maeda, Superstudio The first exhibition for Work at Home situates art, design, and transdisciplinary practices in the home space. In what might be a likely setting for ‘design’, outside of the white cube it presents an alternate context for how we experience contemporary art today. The presentation of ‘art’ and ‘design’ suggests a mutual inclusion of both devices which we use to frame human experience. Beyond ‘home exhibition’ histories, the structure of the visitor experience is as a lived-in space, and presents potentials of what a contemporary collection of art and design might look like today. Presenting in the home creates a new paradigm that explores the evolving publicisation of our private space

The mode of action of the plant antimicrobial peptide MiAMP1 differs from that of its structural homologue, the yeast killer toxin WmKT

The plant antimicrobial peptide MiAMP1 from Macadamia integrifolia and the yeast killer toxin peptide WmKT from Williopsis mrakii are structural homologues. Comparative studies of yeast mutants were performed to test their sensitivity to these two antimicrobial peptides. No differences in susceptibility to MiAMP1 were detected between wild-type and several WmKT-resistant mutant yeast strains. A yeast mutant MT1, resistant to MiAMP1 but unaffected in its susceptibility to plant defensins and hydrogen peroxide, also did not show enhanced tolerance towards WmKT. It is therefore probable that the Greek key beta-barrel structure shared by MiAMP1 and WmKT provides a robust structural framework ensuring stability for the two proteins but that the specific action of the peptides depends on other motifs. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved

Combination of two matrices results in improved performance of MALDI MS for peptide mass mapping and protein analysis.

A new sample preparation method for MALDI based on the use of a mixture of the two commonly used matrices, DHB and CHCA, is described. The matrix mixture preparation results in increased sequence coverage and spot-to-spot reproducibility for peptide mass mapping compared to the use of the single matrix components. This results in more reliable protein identification in proteomics studies and facilitates automated data acquisition. This method shows better tolerance towards salts and impurities, eliminating the need for pre-purification of the samples. It has also been found to be advantageous for the analysis of intact proteins, and especially for glycoproteins. The mixture allows the presence of rather high concentrations of urea in the sample solutions.Journal ArticleResearch Support, Non-U.S. Gov'tinfo:eu-repo/semantics/publishe